Reviewed,
UniProtKB/Swiss-Prot A3KCL7 (OXDD_PIG)
Last modified
October 13, 2009.
Version 19.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: D-aspartate oxidase Short name=DASOX EC=1.4.3.1 Alternative name(s): DDO | ||
| Gene names |
| ||
| Organism | Sus scrofa (Pig) | ||
| Taxonomic identifier | 9823 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 341 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate By similarity. |
| Catalytic activity | D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2. |
| Cofactor | FAD or 6-hydroxyflavin adenine dinucleotide By similarity. |
| Subcellular location | Peroxisome By similarity. |
| Sequence similarities | Belongs to the DAMOX/DASOX family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Peroxisome |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | D-amino-acid oxidase activity Inferred from electronic annotation. Source: InterPro D-aspartate oxidase activityInferred from electronic annotation. Source: EC bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 341 | 341 | D-aspartate oxidase | PRO_0000330729 | |||||
Regions | |||||||||
| Nucleotide binding | 6 – 20 | 15 | FAD By similarity | ||||||
| Nucleotide binding | 36 – 37 | 2 | FAD By similarity | ||||||
| Nucleotide binding | 43 – 44 | 2 | FAD By similarity | ||||||
| Nucleotide binding | 48 – 50 | 3 | FAD By similarity | ||||||
| Nucleotide binding | 307 – 311 | 5 | FAD By similarity | ||||||
| Motif | 339 – 341 | 3 | Microbody targeting signal Potential | ||||||
Sites | |||||||||
| Binding site | 166 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 183 | 1 | FAD By similarity | ||||||
| Binding site | 223 | 1 | Substrate By similarity | ||||||
| Binding site | 278 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Purification, cDNA cloning and characterization of D-aspartate oxidase from porcine kidney." Yamamoto A., Tanaka H., Ishida T., Horiike K. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney. |
Cross-references
Sequence databases | |
|---|---|
| AB271762 mRNA. Translation: BAF47961.1. | |
| RefSeq | NP_001090895.1. |
| UniGene | Ssc.40562 |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 100037287. |
| KEGG | ssc:100037287. |
Organism-specific databases | |
| CTD | 100037287. |
Family and domain databases | |
| InterPro | IPR006181. D-amino_acid_oxidase_CS. IPR006076. FAD-dep_OxRdtase. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF01266. DAO. 1 hit. [Graphical view] |
| PROSITE | PS00677. DAO. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | OXDD_PIG | ||||||||
| Accession | Primary (citable) accession number: A3KCL7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


